BMRB Entry 15806

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR15806

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Title:
1H and 15N Chemical Shift Assignments and Experimental NMR Restraints for the Neurotrypsin Kringle Domain
Deposition date:
2008-06-16
Original release date:
2008-07-02
Authors:
Ozhogina, Olga
Citation:

Citation: Ozhogina, Olga; Grishaev, Alexander; Bominaar, Emile; Llinas, Miguel. "NMR Solution Structure of the Neurotrypsin Kringle Domain"  Biochemistry 47, 12290-12298 (2008).
PubMed: 18956887

Assembly members:

Assembly members:
Neurotrypsin_kringle_domain, polymer, 77 residues, 8533 Da.

Natural source:

Natural source:   Common Name: Norway rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rattus norvegicus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pmed23

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Neurotrypsin_kringle_domain: RCGAGEPWGNATNLGVPCLH WDEVPPFLERSPPASWAELR GQPHNFCRSPDGAGRPWCFY RNAQGKVDWGYCDCGQG

Data sets:
Data typeCount
15N chemical shifts84
1H chemical shifts473

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Neurotrypsin kringle domain1

Entities:

Entity 1, Neurotrypsin kringle domain 77 residues - 8533 Da.

1   ARGCYSGLYALAGLYGLUPROTRPGLYASN
2   ALATHRASNLEUGLYVALPROCYSLEUHIS
3   TRPASPGLUVALPROPROPHELEUGLUARG
4   SERPROPROALASERTRPALAGLULEUARG
5   GLYGLNPROHISASNPHECYSARGSERPRO
6   ASPGLYALAGLYARGPROTRPCYSPHETYR
7   ARGASNALAGLNGLYLYSVALASPTRPGLY
8   TYRCYSASPCYSGLYGLNGLY

Samples:

sample_1: Neurotrypsin, [U-100% 15N], 1 mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_conditions_1: ionic strength: 0.0 mM; pH: 5.2; pressure: 1 atm; temperature: 300.0 K

Experiments:

NameSampleSample stateSample conditions
2D [1H-15N]-HSQCsample_1isotropicsample_conditions_1
2D [1H-15N]-HMBCsample_1isotropicsample_conditions_1
2D [1H-13C]-HSQCsample_1isotropicsample_conditions_1
2D [1H-1H]-TOCSYsample_1isotropicsample_conditions_1
2D [1H-1H]-COSYsample_1isotropicsample_conditions_1
2D [1H-1H]-NOESYsample_1isotropicsample_conditions_1
3D [1H-15N]-NOESYsample_1isotropicsample_conditions_1
3D [1H-15N]-TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1

Software:

ARIA v2.0, Linge, O'Donoghue and Nilges - refinement

ANALYSIS v1.4, CCPN - data analysis

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

FELIX v97, Accelrys Software Inc. - processing

Molmol v2K.2, Koradi, Billeter and Wuthrich - display

ProcheckNMR v3.5.4, Laskowski and MacArthur - geometry plots

QUEEN v1.1, Nabuurs, Spronk, Krieger, Maassen, Vriend and Vuister - quantitative evaluation of experimental distance restraints

NMR spectrometers:

  • Bruker Avance DRX 600 MHz

Related Database Links:

BMRB 15806
PDB
DDBJ Q99JC8
EMBL AJ311671 Q99JC8 CAA73646 CAC35028
GB NP_445956 AAH31429 EDL12300 EDL82129
IUBMB EC: 3.4.21
MEROPS S01.237
NCBI CAC35028 NP_445956
PFAM PF00051
PIR PIRSF037929
REFSEQ NM_053504
SCOP 57441
SWS Q99JC8
UNP Q99JC8
DBJ BAA23986
REF NP_032965 NP_445956
SP G3V801 O08762
AlphaFold Q99JC8 G3V801 O08762

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks